GTPASE MECHANISM OF GPROTEINS FROM THE 1.7-ANGSTROM CRYSTAL STRUCTURE OF TRANSDUCIN ALPHA-GDP-ALF4-

RESIDUES CAC A 353, CAC B 353, AND CAC C 353 MODIFY RESIDUES CYS A 62, CYS B 62, AND CYS C 62, RESPECTIVELY.

RESIDUES CAC A 354, CAC B 354, AND CAC C 354 MODIFY RESIDUES CYS A 210, CYS B 210, AND CYS C 210, RESPECTIVELY.

GTPase mechanism of Gproteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4.

Structural Determinants for Activation of the Alpha-Subunit of a Heterotrimeric G Protein

The 2.2 Angstroms Crystal Structure of Transducin-Alpha Complexed with GTP-Gamma-S

ARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLEECLEFIAIIYGNTLQSILAIVRAMTTLNIQYGDSARQDDARKLMHM
ADTIEEGTMPKEMSDIIQRLWKDSGIQACFDRASEYQLNDSAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGIIETQFS
FKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMHESLHLFNSICNHRYFATTSIVLFLNK
KDVFSEKIKKAHLSICFPDYNGPNTYEDAGNYIKVQFLELNMRRDVKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKD
CGLF

CAC IS DIMETHYL ARSENIC OXIDE, DERIVED FROM CRYSTALLIZATION BUFFER. ALSO KNOWN AS DIMETHYLARSINIC ACID AND CACODYLIC ACID.

THERE ARE THREE COMPLEXES OF TRANSDUCIN ALPHA, GDP,
ALUMINUM FLUORIDE, AND CA 2+ PER ASYMMETRIC UNIT.

MTRIX
THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW
DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE
VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE
MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL
YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED
SECOND.

APPLIED TO TRANSFORMED TO
MTRIX RESIDUES RESIDUES RMSD
M1 C 30 .. C 340 B 30 .. B 340 0.252
M2 C 30 .. C 340 A 30 .. A 340 0.353
M3 B 30 .. B 340 A 30 .. A 340 0.404

GTP-BINDING PROTEIN, G-PROTEIN, GTPASE, TRANSDUCIN

GAGASAEEKHSRELEKKLKEDAEKDARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLEECLEFIAIIYGNTLQSILAIV
RAMTTLNIQYGDSARQDDARKLMHMADTIEEGTMPKEMSDIIQRLWKDSGIQACFDRASEYQLNDSAGYYLSDLERLVTP
GYVPTEQDVLRSRVKTTGIIETQFSFKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMHE
SLHLFNSICNHRYFATTSIVLFLNKKDVFSEKIKKAHLSICFPDYNGPNTYEDAGNYIKVQFLELNMRRDVKEIYSHMTC
ATDTQNVKFVFDAVTDIIIKENLKDCGLF